The c-myc Oncoprotein Forms a Specific Complex with the Product of the Retinoblastoma Gene

  1. A.K. Rustgi*,
  2. N. Dyson,
  3. D. Hill, and
  4. R. Bernards*
  1. Divisions of *Molecular Genetics and Molecular Oncology, The Cancer Center of the Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachusetts 02129; Applied bioTechnology, Cambridge, Massachusetts 02142

This extract was created in the absence of an abstract.

Excerpt

myc proteins are involved in the regulation of cell proliferation and differentiation. Deregulated expression of myc family genes has been implicated in the genesis of a variety of cancers (Lüscher and Eisenman 1990). myc proteins share significant sequence homology in the carboxyl terminus with a number of cellular transcription factors. These basic domain-helix-loop-helix and leucine zipper motifs have been shown to be involved in protein dimerization and DNA binding (Murre et al. 1989; Blackwell et al. 1990; Blackwood and Eisenman 1991). Indeed, evidence now exists to indicate that the c-myc, N-myc, and L-myc proteins can form a heterodimer with a cellular protein, named MAX, and that the myc-MAX heterodimer can bind to DNA in a sequence-specific fashion (Blackwood and Eisenman 1991). In addition, myc proteins have several amino-terminal regions that are highly conserved between myc family members. These regions of homology are not found in other cellular proteins but are...

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